Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Matthijs J. van Haren"'
Autor:
Matthijs J. van Haren, Yongzhi Gao, Ned Buijs, Roberto Campagna, Davide Sartini, Monica Emanuelli, Lukasz Mateuszuk, Agnieszka Kij, Stefan Chlopicki, Pol Escudé Martinez de Castilla, Raymond Schiffelers, Nathaniel I. Martin
Publikováno v:
Biomolecules, Vol 11, Iss 9, p 1357 (2021)
A recently discovered bisubstrate inhibitor of Nicotinamide N-methyltransferase (NNMT) was found to be highly potent in biochemical assays with a single digit nanomolar IC50 value but lacking in cellular activity. We, here, report a prodrug strategy
Externí odkaz:
https://doaj.org/article/fc2a2d1438314007a87c09a76e4ca9c2
Autor:
Yurui Zhang, Matthijs J. van Haren, Nils Marechal, Nathalie Troffer-Charlier, Vincent Cura, Jean Cavarelli, Nathaniel I. Martin
Publikováno v:
Biochemistry, 61(11), 1055-1063. AMER CHEMICAL SOC
Coactivator-associated arginine methyltransferase 1 (CARM1) is a member of the family of protein arginine methyltransferases. CARM1 catalyzes methyl group transfer from the cofactor S-adenosyl-L-methionine (AdoMet) to both histone and nonhistone prot
Publikováno v:
ChemBioChem, 23(24):e202200547. Wiley
The growing threat of drug-resistant bacteria is a global concern, highlighting the urgent need for new antibiotics and antibacterial strategies. In this light, practical synthetic access to natural product antibiotics can provide important structure
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27af3fa0dcab803fd829280f5b689260
https://doi.org/10.1002/cbic.202200547
https://doi.org/10.1002/cbic.202200547
Autor:
Kamaleddin Haj Mohammad Ebrahim Tehrani, Nora C. Brüchle, Nathaniel I. Martin, Ioli Kotsogianni, Vida Mashayekhi, Matthijs J. van Haren, Nicola Wade
Publikováno v:
Chemistry (Weinheim an Der Bergstrasse, Germany)
Chemistry-a European Journal, 27(11), 3806-3811
Chemistry – A European Journal
Chemistry-A European Journal, 27(11), 3806-3811
Chemistry-a European Journal, 27(11), 3806-3811
Chemistry – A European Journal
Chemistry-A European Journal, 27(11), 3806-3811
The increasing prevalence of metallo‐β‐lactamase (MBL)‐expressing bacteria presents a worrying trend in antibiotic resistance. MBLs rely on active site zinc ions for their hydrolytic activity and the pursuit of MBL‐inhibitors has therefore i
Autor:
Agnieszka Kij, Davide Sartini, Roberto Campagna, Nathaniel I. Martin, Monica Emanuelli, Seino A. K. Jongkees, Ned Buijs, Matthijs J. van Haren, Yurui Zhang, Filip A. Fedak, Stefan Chlopicki, Yongzhi Gao, Lukasz Mateuszuk, Vito Thijssen
Publikováno v:
RSC Chemical Biology, 2(5), 1546-1555
RSC Chemical Biology, 2(5), 1546-1555. Royal Society of Chemistry
Van Haren, M J, Zhang, Y, Thijssen, V, Buijs, N, Gao, Y, Mateuszuk, L, Fedak, F A, Kij, A, Campagna, R, Sartini, D, Emanuelli, M, Chlopicki, S, Jongkees, S A K & Martin, N I 2021, ' Macrocyclic peptides as allosteric inhibitors of nicotinamide : N-methyltransferase (NNMT) ', RSC Chemical Biology, vol. 2, no. 5, pp. 1546-1555 . https://doi.org/10.1039/d1cb00134e
RSC Chemical Biology, 2(5), 1546-1555. Royal Society of Chemistry
Van Haren, M J, Zhang, Y, Thijssen, V, Buijs, N, Gao, Y, Mateuszuk, L, Fedak, F A, Kij, A, Campagna, R, Sartini, D, Emanuelli, M, Chlopicki, S, Jongkees, S A K & Martin, N I 2021, ' Macrocyclic peptides as allosteric inhibitors of nicotinamide : N-methyltransferase (NNMT) ', RSC Chemical Biology, vol. 2, no. 5, pp. 1546-1555 . https://doi.org/10.1039/d1cb00134e
Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-Adenosyl-l-methionine (SAM) as the methyl donor. The complexity of the role of NNMT in healthy and disease states is slowly being elucidated an
Publikováno v:
Methods
Methods, 175, 24-29
Methods, 175, 24-29
Protein arginine N-methyltransferases (PRMTs) methylate arginine residues in target proteins using the ubiquitous methyl donor S-adenosyl-l-methionine (AdoMet) as a cofactor. PRMTs play important roles in both healthy and disease states and as such i
Autor:
Nathaniel I. Martin, Nils Marechal, Matthijs J. van Haren, Yurui Zhang, Nathalie Troffer-Charlier, V. Cura, Jean Cavarelli
Publikováno v:
'ChemBioChem ', vol: 22, pages: 3469-3476 (2021)
ChemBioChem, 22(24), 3469-3476
ChemBioChem, 22(24), 3469-3476
The dynamic interplay of post-translational modifications (PTMs) in chromatin provides a communication system for the regulation of gene expression. An increasing number of studies have highlighted the role that such crosstalk between PTMs plays in c
Autor:
Nathaniel I. Martin, Agnieszka Kij, Lukasz Mateuszuk, Monica Emanuelli, Ned Buijs, Stefan Chlopicki, Roberto Campagna, Yongzhi Gao, Matthijs J. van Haren, Raymond M. Schiffelers, Pol Escudé Martinez de Castilla, Davide Sartini
Publikováno v:
Biomolecules
Biomolecules, 11(9)
Biomolecules, Vol 11, Iss 1357, p 1357 (2021)
Volume 11
Issue 9
Biomolecules, 11(9)
Biomolecules, Vol 11, Iss 1357, p 1357 (2021)
Volume 11
Issue 9
A recently discovered bisubstrate inhibitor of Nicotinamide N-methyltransferase (NNMT) was found to be highly potent in biochemical assays with a single digit nanomolar IC50 value but lacking in cellular activity. We, here, report a prodrug strategy
Autor:
Matthijs J, van Haren, Yurui, Zhang, Vito, Thijssen, Ned, Buijs, Yongzhi, Gao, Lukasz, Mateuszuk, Filip A, Fedak, Agnieszka, Kij, Roberto, Campagna, Davide, Sartini, Monica, Emanuelli, Stefan, Chlopicki, Seino A K, Jongkees, Nathaniel I, Martin
Publikováno v:
RSC Chemical Biology
Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide to form 1-methylnicotinamide (MNA) using S-adenosyl-l-methionine (SAM) as the methyl donor. The complexity of the role of NNMT in healthy and disease states is slowly being elucidated an
Publikováno v:
Drug Discovery Today, 26(11), 2699-2706
Nicotinamide N-methyltransferase (NNMT) methylates nicotinamide (NA) to generate 1-methyl nicotinamide. Since its discovery 70 years ago, the appreciation of the role of NNMT in human health has evolved from serving only metabolic functions to also b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ffaa2d6ae58cac9fac8b4aab8f55d86
https://doi.org/10.1016/j.drudis.2021.05.011
https://doi.org/10.1016/j.drudis.2021.05.011